Results 231 to 240 of about 61,173 (287)
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2013
Antithrombin (AT) is a heparin cofactor and a member of the serine protease inhibitor family (serpin). The mature AT molecule is composed of 432 amino acids and it is produced mainly in the liver. Initially, several different AT activities in plasma were reported, leading to the classification of antithrombin in a range from I to IV.
Mirta, Hepner, Vasiliki, Karlaftis
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Antithrombin (AT) is a heparin cofactor and a member of the serine protease inhibitor family (serpin). The mature AT molecule is composed of 432 amino acids and it is produced mainly in the liver. Initially, several different AT activities in plasma were reported, leading to the classification of antithrombin in a range from I to IV.
Mirta, Hepner, Vasiliki, Karlaftis
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Management of antithrombin deficiency: an update for clinicians
Expert Review of Hematology, 2019Introduction. Antithrombin is a serpin that inhibits multiple procoagulant serine proteases and acts as an endogenous anticoagulant. Thus, congenital antithrombin deficiency constitutes a major thrombophilic state, the most severe so far.
C. Bravo-Pérez, V. Vicente, J. Corral
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Seminars in Thrombosis and Hemostasis, 2007
Angiogenesis is critical for several physiologic and pathophysiologic processes, and several angiogenesis inhibitors are now in clinical trials for the treatment of cancer. Antithrombin is a member of the serpin family of proteins and functions as an inhibitor of thrombin and other enzymes involved in the clotting cascade. While studying the inhibition
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Angiogenesis is critical for several physiologic and pathophysiologic processes, and several angiogenesis inhibitors are now in clinical trials for the treatment of cancer. Antithrombin is a member of the serpin family of proteins and functions as an inhibitor of thrombin and other enzymes involved in the clotting cascade. While studying the inhibition
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Thrombosis and Haemostasis, 1971
SummaryAn evaluation of the mode of action of antithrombin in the temporary inhibition of purified 3.7 S bovine thrombin was made according to traditional enzyme inhibition theory. Using enzyme clotting activity and concentration of active sites synonymously, it was observed that the binding of antithrombin to thrombin followed a second order reaction ...
Frederick A. Dombrose +2 more
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SummaryAn evaluation of the mode of action of antithrombin in the temporary inhibition of purified 3.7 S bovine thrombin was made according to traditional enzyme inhibition theory. Using enzyme clotting activity and concentration of active sites synonymously, it was observed that the binding of antithrombin to thrombin followed a second order reaction ...
Frederick A. Dombrose +2 more
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Platelet antithrombin activity
Thrombosis Research, 1980Abstract Platelets were studied for the presence of antithrombin (thrombin amidolytic inhibitory) activity. Platelet rich plasma contained more antithrombin activity than platelet poor plasma. This activity could be washed from a platelet pellet. Antithrombin activity increased on sonication of platelets but not following aggregation.
E E, Czapek, H C, Kwaan
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JAMA: The Journal of the American Medical Association, 1978
To the Editor.— In a recent letter to the editor, Rodger L. Bick, MD, commented on methods of assay of antithrombin III (239:296, 1978), pointing out several drawbacks to the use of synthetic chromogenic substrates in such assays. His comments were prompted by an article in MEDICAL NEWS (238:1005, 1977) in which we reported that these peptides were ...
H L, Messmore, J, Fareed
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To the Editor.— In a recent letter to the editor, Rodger L. Bick, MD, commented on methods of assay of antithrombin III (239:296, 1978), pointing out several drawbacks to the use of synthetic chromogenic substrates in such assays. His comments were prompted by an article in MEDICAL NEWS (238:1005, 1977) in which we reported that these peptides were ...
H L, Messmore, J, Fareed
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Molecular Medicine Today, 1995
Antithrombin, the main inhibitor of thrombosis in blood, is bound and activated by the heparin-like side-chains that line the small vasculature. We now have good depictions of the heparin-binding site on antithrombin, and of the way in which mutations at this site cause thrombotic disease.
R, Carrell +3 more
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Antithrombin, the main inhibitor of thrombosis in blood, is bound and activated by the heparin-like side-chains that line the small vasculature. We now have good depictions of the heparin-binding site on antithrombin, and of the way in which mutations at this site cause thrombotic disease.
R, Carrell +3 more
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British Journal of Haematology, 1984
SummaryAntithrombin III (AT‐III) heparin cofactor activity and its antigen levels have been determined in 106 plasma samples from 42 term and preterm neonates. In contrast to healthy adult controls, a reduced activity/antigen (act/ag) ratio (ranging from 0‐26 to 0‐86) was observed in 90% of the samples and was independent of the state of health of the ...
Peters, M. +5 more
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SummaryAntithrombin III (AT‐III) heparin cofactor activity and its antigen levels have been determined in 106 plasma samples from 42 term and preterm neonates. In contrast to healthy adult controls, a reduced activity/antigen (act/ag) ratio (ranging from 0‐26 to 0‐86) was observed in 90% of the samples and was independent of the state of health of the ...
Peters, M. +5 more
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Hirudins: Antithrombin Anticoagulants
Annals of Pharmacotherapy, 1992OBJECTIVE: To review the chemistry, pharmacology, available clinical data, and adverse effects of the hirudin anticoagulants. DATA SOURCES: A MEDLINE search and a review of recent scientific abstracts was conducted to identify pertinent literature. STUDY SELECTION: Focus was placed on studies conducted in humans.
K A, Stringer, J, Lindenfeld
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Commercial Antithrombin Concentrate Contains Inactive L-forms of Antithrombin
Thrombosis and Haemostasis, 1997SummaryThe preparation of antithrombin concentrate for clinical use requires a viral inactivation step. In most commercial preparations this is achieved by heat pasteurisation. This process would be expected to alter the conformation of antithrombin from the active native species to an inactive latent (L-form) state (1, 2).
W S, Chang, P L, Harper
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